Extraction, purification and characterization of papain enzyme from papaya

Abstract

Papain is one of the widely used enzymes in the industry. This study aimed to extract papain enzyme from various parts (i.e. latex, leaves, peels and seeds) of papaya using distilled water and citric phosphate buffer and subsequently purified with a two-step salt precipitation method. The optimum protein concentration of purified papain was obtained with citric phosphate buffer (0.159-0.319 mg/mL) and distilled water (0.119-0.347 mg/ mL). The protein concentration was almost similar for crude extracted with both the solvent. The purification procedure enhanced up to 1.56 fold when extracted with distilled water and 0.83 fold when extracted with citric phosphate buffer. Latex, leaves, peels and seeds showed maximum enzyme activity at 60oC and pH 8.0 as well as better thermal stability at 60oC for 30 mins. Findings highlighted that extracted papain enzyme from waste parts of papaya could be utilized as a potential source of industrial application in terms of waste to value-added products.